ArticleCell death & disease2013
Pathogenic prions deviate PrP(C) signaling in neuronal cells and impair A-beta clearance.
Article in Cell death & disease, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 29 citations in OpenAlex.
- Post-translational modifications in prion diseases.Frontiers in molecular neuroscience · 2024Review
- Article
- Loss of prion protein control of glucose metabolism promotes neurodegeneration in model of prion diseases.PLoS pathogens · 2021Article
- The Cellular Prion Protein-ROCK Connection: Contribution to Neuronal Homeostasis and Neurodegenerative Diseases.Frontiers in cellular neuroscience · 2021Review
- The Link of the Prion Protein with CaInternational journal of molecular sciences · 2019Review
- Production of seedable Amyloid-β peptides in model of prion diseases upon PrPNature communications · 2019Article
- Epigenetic Control of the Notch and Eph Signaling Pathways by the Prion Protein: Implications for Prion Diseases.Molecular neurobiology · 2019Article
- GPI-anchor signal sequence influences PrPC sorting, shedding and signalling, and impacts on different pathomechanistic aspects of prion disease in mice.PLoS pathogens · 2019Article
- Attempt to Untangle the Prion-Like Misfolding Mechanism for Neurodegenerative Diseases.International journal of molecular sciences · 2018Review
- Protective role of cellular prion protein against TNFα-mediated inflammation through TACE α-secretase.Scientific reports · 2017Article
- Secretory pathway retention of mutant prion protein induces p38-MAPK activation and lethal disease in mice.Scientific reports · 2016Article
- Cu(II)-Zn(II) Cross-Modulation in Amyloid-Beta Peptide Binding: An X-ray Absorption Spectroscopy Study.The journal of physical chemistry. B · 2015Article
- Activation of the AMPK-ULK1 pathway plays an important role in autophagy during prion infection.Scientific reports · 2015Article
- Article
- Prion diseases and adult neurogenesis: how do prions counteract the brain's endogenous repair machinery?Prion · 2014Article
- Review
- PrP(C) from stem cells to cancer.Frontiers in cell and developmental biology · 2014Review
- Hijacking PrP(c)-dependent signal transduction: when prions impair Aβ clearance.Frontiers in aging neuroscience · 2014Review
- PDK1 decreases TACE-mediated α-secretase activity and promotes disease progression in prion and Alzheimer's diseases.Nature medicine · 2013Article
- Article
Corrections and comments
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Authors and funding
11 authors at 6 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The subversion of the normal function exerted by the cellular prion protein (PrP(C)) in neurons by pathogenic prions is assumed to have a central role in the pathogenesis of transmissible spongiform encephalopathies. Using two murine models of prion infection, the 1C11 neuronal cell line and neurospheres, we document that prion infection is associated with the constitutive activation of signaling targets normally coupled with PrP(C), including the Fyn kinase, the mitogen-associated protein kinases ERK1/2 and the CREB transcription factor. PrP(C)-dependent signaling overactivation in infected cells is associated with the recruitment of p38 and JNK stress-associated kinases. Downstream from CREB, prion-infected cells exhibit reduced activity of the matrix metalloprotease (MMP)-9. As MMP-9 catalyzes the degradation of the amyloid A-beta peptide, the decrease in MMP-9 activity in prion-infected cells causes a significant impairment of the clearance of A-beta, leading to its accumulation. By exploiting two 1C11-infected clones accumulating high or moderate levels of prions, we show that the prion-induced changes are correlated with the level of infectivity. Of note, a dose-dependent increase in A-beta levels was also found in the cerebrospinal fluid of mice inoculated with these infected clones. By demonstrating that pathogenic prions trigger increases in A-beta levels through the deviation of PrP(C) signaling, our data argue that A-beta may exacerbate prion-induced toxicity.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.